Ebola virus glycoprotein GP1,2 (GP1,2)

The Ebola virus glycoprotein GP1,2 is the sole protein expressed on the surface of the Ebola virus virion and is essential for viral entry into host cells (UniProt) [1.4.1]. It is synthesized as a precursor (GP0) that is cleaved by furin into two subunits, GP1 and GP2, which remain linked by a disulfide bond to form a trimeric spike (NIH) [1.2.3]. GP1 is responsible for attachment to host cell receptors, such as NPC1 in the endosome, while GP2 mediates the fusion of the viral envelope with the host cell membrane (PubMed) [1.1.1]. Beyond its role in entry, GP1,2 contributes to pathogenesis through immune evasion—using a dense glycan shield and producing a secreted isoform (sGP) that acts as a decoy for antibodies—and by inducing cytotoxicity and vascular permeability (NIH) [1.2.2, 1.3.1]. As the primary target for the host's neutralizing antibody response, GP1,2 is the focus of vaccine development (e.g., rVSV-ZEBOV) and monoclonal antibody therapies (e.g., Inmazeb and Ebanga) that aim to block viral infection (FDA, Nature Reviews) [1.2.1, 1.2.4].

Other names

Envelope glycoproteinGPEBOV GPEBGPSpike proteinGP1/GP2

Neutralization of viral entry by binding to the glycoprotein and preventing attachment to host receptors (e.g., NPC1) or inhibiting the conformational changes required for membrane fusion (Nature Reviews) [1.2.4].